John E. Pak

5.7k total citations · 2 hit papers
31 papers, 1.7k citations indexed

About

John E. Pak is a scholar working on Molecular Biology, Infectious Diseases and Immunology. According to data from OpenAlex, John E. Pak has authored 31 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 10 papers in Infectious Diseases and 7 papers in Immunology. Recurrent topics in John E. Pak's work include SARS-CoV-2 and COVID-19 Research (8 papers), Glycosylation and Glycoproteins Research (5 papers) and SARS-CoV-2 detection and testing (4 papers). John E. Pak is often cited by papers focused on SARS-CoV-2 and COVID-19 Research (8 papers), Glycosylation and Glycoproteins Research (5 papers) and SARS-CoV-2 detection and testing (4 papers). John E. Pak collaborates with scholars based in United States, Canada and India. John E. Pak's co-authors include Xiaohui Deng, William A. Müller, Payton A. Weidenbacher, Peter S. Kim, Shaogeng Tang, Wesley Wu, James M. Rini, Ellen Shapiro, Tung‐Tien Sun and Xue‐Ru Wu and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

John E. Pak

30 papers receiving 1.6k citations

Hit Papers

Efficient evolution of human antibodies from general prot... 2023 2026 2024 2025 2023 2025 50 100 150 200

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
John E. Pak United States 18 837 362 306 252 194 31 1.7k
Antonella Bugatti Italy 28 941 1.1× 280 0.8× 325 1.1× 92 0.4× 108 0.6× 75 1.9k
Chiara Urbinati Italy 29 1.3k 1.6× 140 0.4× 420 1.4× 103 0.4× 215 1.1× 55 2.1k
Øystein Garred Norway 20 1.1k 1.4× 256 0.7× 469 1.5× 81 0.3× 64 0.3× 43 2.2k
Marko Fonovič Slovenia 24 1.5k 1.8× 65 0.2× 203 0.7× 176 0.7× 158 0.8× 49 2.7k
Regina Heidenreich Germany 26 1.7k 2.1× 316 0.9× 956 3.1× 107 0.4× 69 0.4× 44 2.7k
Ricardo J. Giordano Brazil 24 1.2k 1.4× 47 0.1× 262 0.9× 475 1.9× 104 0.5× 51 2.1k
Benjamin G. Hoffstrom United States 14 1.2k 1.4× 449 1.2× 215 0.7× 89 0.4× 352 1.8× 22 2.3k
Tiina Öhman Finland 22 924 1.1× 109 0.3× 357 1.2× 53 0.2× 58 0.3× 36 1.5k
Silke Hoffmann Germany 23 830 1.0× 134 0.4× 110 0.4× 122 0.5× 140 0.7× 63 1.6k
William A. Rees United States 23 852 1.0× 77 0.2× 1.2k 3.8× 116 0.5× 187 1.0× 59 2.7k

Countries citing papers authored by John E. Pak

Since Specialization
Citations

This map shows the geographic impact of John E. Pak's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by John E. Pak with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites John E. Pak more than expected).

Fields of papers citing papers by John E. Pak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John E. Pak. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by John E. Pak. The network helps show where John E. Pak may publish in the future.

Co-authorship network of co-authors of John E. Pak

This figure shows the co-authorship network connecting the top 25 collaborators of John E. Pak. A scholar is included among the top collaborators of John E. Pak based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with John E. Pak. John E. Pak is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
2.
Tang, Shaogeng, Soohyun Kim, Varun R. Shanker, et al.. (2025). Utilizing Machine Learning to Improve Neutralization Potency of an HIV-1 Antibody Targeting the gp41 N-Heptad Repeat. ACS Chemical Biology. 20(7). 1470–1480. 1 indexed citations
3.
Swanson, Kyle, et al.. (2025). The Virtual Lab of AI agents designs new SARS-CoV-2 nanobodies. Nature. 646(8085). 716–723. 18 indexed citations breakdown →
4.
Wu, Wesley, Sasha Gupta, Sharon A. Sagan, et al.. (2024). High-yield production of recombinant human myelin oligodendrocyte glycoprotein in SHuffle bacteria without a refolding step. Journal of Immunological Methods. 534. 113764–113764. 1 indexed citations
5.
Hie, Brian, Varun R. Shanker, Duo Xu, et al.. (2023). Efficient evolution of human antibodies from general protein language models. Nature Biotechnology. 42(2). 275–283. 205 indexed citations breakdown →
6.
Shoemaker, Sophie R., et al.. (2023). Exploring the conformational landscape of the rabies virus glycoprotein using HDX-MS. Biophysical Journal. 122(3). 189a–189a. 1 indexed citations
7.
Gupta, Sasha, Milos Simic, Sharon A. Sagan, et al.. (2023). CAR-T Cell–Mediated B-Cell Depletion in Central Nervous System Autoimmunity. Neurology Neuroimmunology & Neuroinflammation. 10(2). 46 indexed citations
8.
Shoemaker, Sophie R., et al.. (2023). Epitope mapping of diagnostic anti-rabies monoclonal antibodies provide structural insight into rabies variant identification in infected wildlife. Biophysical Journal. 122(3). 331a–331a. 1 indexed citations
9.
Weidenbacher, Payton A., Eric Waltari, Mary Kate Morris, et al.. (2022). Converting non-neutralizing SARS-CoV-2 antibodies into broad-spectrum inhibitors. Nature Chemical Biology. 18(11). 1270–1276. 13 indexed citations
10.
Costello, Shawn M., Sophie R. Shoemaker, Annalee W. Nguyen, et al.. (2022). The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes. Nature Structural & Molecular Biology. 29(3). 229–238. 74 indexed citations
11.
Waltari, Eric, et al.. (2022). AIRRscape: An interactive tool for exploring B-cell receptor repertoires and antibody responses. PLoS Computational Biology. 18(9). e1010052–e1010052. 3 indexed citations
12.
Powell, Abigail E., Kaiming Zhang, Mrinmoy Sanyal, et al.. (2021). A Single Immunization with Spike-Functionalized Ferritin Vaccines Elicits Neutralizing Antibody Responses against SARS-CoV-2 in Mice. ACS Central Science. 7(1). 183–199. 122 indexed citations
13.
Eriksen, Jacob, Narinobu Juge, John E. Pak, et al.. (2019). Structures suggest a mechanism for energy coupling by a family of organic anion transporters. PLoS Biology. 17(5). e3000260–e3000260. 38 indexed citations
14.
Li, Zhijie, et al.. (2017). Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1. Nature Chemical Biology. 13(7). 757–763. 62 indexed citations
15.
Chaudhary, Sarika, John E. Pak, Franz Gruswitz, Vinay Sharma, & Robert M. Stroud. (2012). Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells. Nature Protocols. 7(3). 453–466. 63 indexed citations
16.
Pak, John E., Malathy Satkunarajah, J. Seetharaman, & James M. Rini. (2011). Structural and Mechanistic Characterization of Leukocyte-Type Core 2 β1,6-N-Acetylglucosaminyltransferase: A Metal-Ion-Independent GT-A Glycosyltransferase. Journal of Molecular Biology. 414(5). 798–811. 16 indexed citations
17.
Pak, John E., Chetna Sharon, Malathy Satkunarajah, et al.. (2009). Structural Insights into Immune Recognition of the Severe Acute Respiratory Syndrome Coronavirus S Protein Receptor Binding Domain. Journal of Molecular Biology. 388(4). 815–823. 41 indexed citations
18.
Pak, John E. & James M. Rini. (2006). X‐ray Crystal Structure Determination of Mammalian Glycosyltransferases. Methods in enzymology on CD-ROM/Methods in enzymology. 416. 30–48. 8 indexed citations
19.
Smith, Sallie W., et al.. (1999). Characterization of a mutant T-cell hybridoma line with defects in the TCR-mediated apoptotic pathway. Cell Death and Differentiation. 6(1). 36–47. 3 indexed citations
20.
Pak, John E., et al.. (1994). Monoclonal antibody to murine PECAM-1 (CD31) blocks acute inflammation in vivo.. The Journal of Experimental Medicine. 179(3). 1059–1064. 264 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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